Recombinant Human TIMP3 Proteins
- Known as:
- Recombinant Human TIMP3 Proteins
- Catalog number:
- RB-15-0001P-10
- Product Quantity:
- 10
- Category:
- -
- Supplier:
- Ray Biotech
- Gene target:
- Recombinant Human TIMP3 Proteins
Related genes to: Recombinant Human TIMP3 Proteins
- Gene:
- TIMP3 NIH gene
- Name:
- TIMP metallopeptidase inhibitor 3
- Previous symbol:
- SFD
- Synonyms:
- -
- Chromosome:
- 22q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1993-04-12
- Date modifiied:
- 2014-11-19
Related products to: Recombinant Human TIMP3 Proteins
Related articles to: Recombinant Human TIMP3 Proteins
- DNA methylation of tumour suppressor genes is the most well-studied epigenetic alterations in head and neck cancer. The tumour suppressor genes CDKN2A, RASSF1, and TIMP3 are the most frequently investigated, but the methylation status has been analysed in more than another dozen genes, for example MGMT. In oral squamous cell carcinoma (OSCC) methylation of MGMT, DAPK, and CDKN2A are promising biomarkers of prognostic value. Inhibition of LSD1, encoding a histone demethylase, attenuates the development and growth of OSCC. Methylation of TIMP3 in sinonasal adenocarcinoma (intestinal type) is associated with a significant worse survival, an association not seen in sinonasal squamous cell carcinoma. Olfactory neuroblastoma can be distinguished into four unique subgroups by methylation profiling. Methylation of RASSF1 is seen in NUT carcinoma, and significantly higher RASSF1 methylation is found in SMARCB1/INI1-deficient tumours compared to the less aggressive SMARCB1/INI-proficient tumours. Genome-wide methylation profiling in combination with IDH2 mutation status suggests that tumours with undifferentiable SNUC morphology can be classified into for subgroups. Most salivary gland carcinoma subtypes have specific epigenetic signatures. Four of the most common subtypes, adenoid cystic carcinoma (ADCC), mucoepidermoid carcinoma (MEC), acinic cell carcinoma (ACC), and carcinoma ex pleomorphic adenoma (CXPA) have all methylation of RASSF1A, two (MEC and ADCC) also of TIMP3 and two (MEC and CXPA) of p16INK. A methylation landscape of 20 salivary gland tumours (SGTs) is nowadays available. - Source: PubMed
Publication date: 2026/04/29
Hellquist HenrikCastelo-Branco PedroStenman GöranNadal AlfonsAgaimy AbbasZidar Ninade Lima-Souza Reydson AlcidesMariano Fernanda VivianeCoca-Pelaz AndrésFerlito Alfio - Chronic kidney disease (CKD) is a systemic condition associated with inflammation and oxidative stress, affecting organs beyond the kidneys. Although rarely emphasized, the eyes may also be affected but underlying molecular mechanisms remain largely unexplored. The gut-kidney and gut-eye axes are emerging as therapeutic targets with prebiotics like ResistAid®-a Larch Arabinogalactan (LAG) supplement with antioxidant and immunomodulatory effects-showing promise through gut microbiota modulation. This study assessed ResistAid®'s effects on ocular gene expression in a CKD rat model. Twenty four Wistar rats were assigned to Sham (S), Sham + Treatment (ST), Nephrectomized (N), Nephrectomized + Treatment (NT) ( = 6 each). CKD was induced by 5/6 nephrectomy. The treatment was administered via gavage for 30 days at a dose of 5.35 mg/day, adapted from human recommendations. At day 30, blood and tissues were collected. Expression of antioxidant enzymes () and other genes () was analyzed by qPCR. Biochemical and well-being assessments were also conducted. Nephrectomy, regardless of treatment, increased and expression in eye and blood; Specific to NT animals, ocular , and expressions were markedly elevated when compared with N animals and blood and ocular expressions were not elevated, differing from N animals. No significant changes were observed between the S and ST groups. CKD induces systemic oxidative and inflammatory responses. ResistAid® partially mitigated these effects in blood and eye, suggesting systemic and local benefits, possibly via gut microbiota modulation. - Source: PubMed
Publication date: 2026/04/29
Alves Reis Pedro HenriqueDestro Isabela de PaulaLamy Ingrid BertolliniPetri GiulianaSilvestri Estella FreitasTrufelli Isabella Dudjak RosaAlves Beatriz da Costa AguiarLima Vagner Loducada Veiga Glaucia LucianoFonseca Fernando Luiz Affonso - Bothrops envenomation induces extensive local tissue destruction and a robust inflammatory response, largely driven by the host's endogenous molecular pathways. Among these, Matrix Metalloproteinases (MMPs), zinc-dependent endopeptidases responsible for extracellular matrix (ECM) degradation, play a central role. The clinical severity of envenomation is therefore strongly influenced by the balance between MMPs and their specific inhibitors, the TIMPs. This study investigated the contribution of MMP-1, MMP-2, MMP-7, MMP-9, and MMP-10 and TIMP-1, TIMP-2, TIMP-3, and TIMP-4 to the inflammatory response following Bothrops snakebites. - Source: PubMed
Publication date: 2026/04/24
Ferreira Neves Juliana CostaMagalhães-Gama FábioIbiapina Hiochelson Najibe SantosSeixas Kamille BeltrãoBarbosa Êndila SouzaMalheiro AdrianaSachett Jacqueline Almeida GonçalvesCampi-Azevedo Ana CarolinaMartins-Filho Olindo AssisTeixeira-Carvalho AndréaSartim Marco AurélioMonteiro WueltonCosta Allyson Guimarães - Objective This study aimed to investigate the protective effect of a metformin (Met)-adipose-derived mesenchymal stem cell exosome (ADSC-Exo) complex (Met-Exo) against hepatic ischemia-reperfusion injury (IRI) and to determine whether this protection is mediated through the silent information regulator 1(SIRT1)-tissue inhibitor of metalloproteinase 3(TIMP3) axis. Methods Met-Exo was constructed and characterized by nanoparticle tracking analysis, Western blotting, and transmission electron microscopy (TEM). An in vitro model of hepatic IRI was established in mouse hepatocyte AML12 cells subjected to oxygen-glucose deprivation/re-oxygenation (OGD/R). Cell viability, apoptosis, and hepatocyte function markers (AST and ALT) were measured to compare the protective effects of Met-Exo, ADSC-Exo, and Met alone. A Transwell co-culture system was used to evaluate how macrophage polarization influences OGD/R-induced AML12 injury. AML12 cells were assigned to the following groups: Ctrl, OGD/R, Met, ADSC-Exo, Met-Exo, and macrophage-polarization groups (M0, M1, M1+Met-Exo, M1+pcDNA3.1, M1+pcDNA3.1-SIRT1, M1+pcDNA3.1-TIMP3). SIRT1 and TIMP3 protein levels in AML12 cells were determined by Western blot. Macrophage-polarization markers-inducible nitric-oxide synthase (iNOS) and arginase 1 (Arg1) were also quantified. In parallel, AML12 cells' viability, apoptosis, and hepatocellular function indices (AST& ALT) were assessed. A murine hepatic IRI model was constructed, and Met-Exo was administered to assess therapeutic efficacy in vivo. Results Met-Exo was successfully prepared. In vitro, Met-Exo attenuated OGD/R-induced hepatocyte injury, increased viability, reduced apoptosis, and lowered AST and ALT release. Met-Exo pre-treatment suppressed expression of the M1 marker iNOS and enhanced expression the M2 marker Arg1, thereby alleviating OGD/R damage in AML12 cells. OGD/R markedly decreased SIRT1 and TIMP3 expression in AML12 cells, whereas Met-Exo pre-treatment significantly up-regulated SIRT1 and consequently TIMP3 expression. In macrophage polarization experiments, M1 macrophages exacerbated AML12 injury, shown as decreased protein expression of SIRT1 and TIMP3, increased iNOS levels, reduced Arg1 levels, along with diminished AML12 cell viability, increased apoptosis, and elevated AST/ALT. Over-expression of either SIRT1 or TIMP3 reversed these detrimental effects, skewing macrophages toward the M2 phenotype and mitigating AML12 injury. In vivo, Met-Exo markedly ameliorated hepatic IRI in mice. Conclusion Met-Exo protects against hepatic IRI by activating the SIRT1-TIMP3 axis, thereby driving macrophage polarization toward the anti-inflammatory M2 phenotype, attenuating inflammation and apoptosis in hepatocytes subjected to OGD/R. - Source: PubMed
Jiang AiwenPu JiekunZhao XuepingZhang YiNiu CongChen Yong - Tissue inhibitor of metalloproteinase 3 (TIMP-3) is a broad-spectrum inhibitor of matrix metalloproteinases (MMPs) and ADAM/ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family enzymes that regulate extracellular matrix (ECM) homeostasis. Because these enzymes play key roles in articular cartilage turnover, TIMP-3-mediated inhibition protects against cartilage degradation, a hallmark of osteoarthritis (OA), and has been explored as a therapeutic target. Nonetheless, unexpected detrimental effects of TIMP-3 on bone mass and structure have been reported in transgenic mice overexpressing TIMP-3 in cartilage. Mechanistically, TIMP-3 binds catabolic enzymes and blocks their active sites but also interacts with low-density lipoprotein receptor-related protein 1 (LRP-1) and sulfated proteoglycans in the ECM, processes that regulate its half-life through a balance between endocytosis and ECM retention and may influence cell signaling. - Source: PubMed
Publication date: 2026/03/11
Mengozzi ManuelaTowler BenKwabiah JordanRazmandeh FawadSimoes FabioMullen Lisa